CRYSTALLOGRAPHIC STUDIES OF ENZYME MECHANISMS

酶机制的晶体学研究

• 批准号: 6119528
• 负责人: ALLEN M ORVILLE
• 金额: --
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1999
• 资助国家: 美国
• 起止时间: 1999-03-01 至 2000-04-14
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6119528
• 关键词: biomaterials; proteins; structural biology

The following projects are aimed at obtaining insights into reaction mechanisms through structural analysis of enzymes and their inhibitor complexes. These high resolution studies should not only determine locations of inhibitors and transition state analogs but also potentially important solvent molecules. In the case of Nitroglycerine Reductase we are attempting to determine the fold of a novel enzyme for which no structure is presently available. The projects include: _-galactosidase, Methionine Aminopeptidase and Nitroglycerine Reductase.

以下项目旨在深入了解 通过酶的结构分析反应机理及其 抑制剂复合物。 这些高分辨率的研究不仅应该 确定抑制剂和过渡态类似物的位置， 也是潜在重要的溶剂分子。 的情况下 硝酸甘油还原酶，我们试图确定折叠的 目前还没有结构可用的新酶。 的 项目包括：_-半乳糖苷酶，甲氨酰氨肽酶和 硝酸甘油还原酶。